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Q6MAC7 (GSA_PARUW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate-1-semialdehyde 2,1-aminomutase

Short name=GSA
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT
Gene names
Name:hemL
Ordered Locus Names:pc1748
OrganismProtochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]
Taxonomic identifier264201 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00375

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243593

Amino acid modifications

Modified residue2711N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MAC7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 3E3D1C614275D0D5

FASTA43247,738
        10         20         30         40         50         60 
MISRPISQQI YSNLNRVIPG GVNSPVRACA NMGQIPMIID HAYRDTLVDV DGKTYVDYCG 

        70         80         90        100        110        120 
SWGALIHGHA HPSILEAVQQ RMKKGTSFGI TTSIEGELAQ EVIKLIDSVE KIRFVSSGTE 

       130        140        150        160        170        180 
ATMSAVRLAR GYTNKEFIVK FNGNYHGHAD FFLVQAGSGV LEVSPSASSA GIPADIVKQT 

       190        200        210        220        230        240 
LCLPYNDIEA CRQIFHHSDY RHKIAAIILE PIAGNMGVIP ASQEFMQFLR KETLAMGALL 

       250        260        270        280        290        300 
IFDEVMTGFR VALKGAQDIY PVEPDLTCFG KIIGGGFPAA AFGGREEIMN LLAPLGSVYQ 

       310        320        330        340        350        360 
AGTLSGNPIA MEAGLQSLRL IQQPGFYEEL HRKTDLLLNP IKETIKKNNW PICIQQAGSM 

       370        380        390        400        410        420 
FTLFFCKNRV RNLEDALKAN TTIFANFFRK LFDQGIYIPP SQHEAWFISQ AHEESNLIKT 

       430 
QSAILTFLEE NF 

« Hide

References

[1]"Illuminating the evolutionary history of chlamydiae."
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.
Science 304:728-730(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UWE25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX908798 Genomic DNA. Translation: CAF24472.1.
RefSeqYP_008747.1. NC_005861.1.

3D structure databases

ProteinModelPortalQ6MAC7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264201.pc1748.

Proteomic databases

PRIDEQ6MAC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF24472; CAF24472; pc1748.
GeneID2781344.
KEGGpcu:pc1748.
PATRIC31998930. VBICanPro72727_1794.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycPAMO264201:GH0M-1784-MONOMER.
UniPathwayUPA00251; UER00317.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00375. HemL_aminotrans_3.
InterProIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_PARUW
AccessionPrimary (citable) accession number: Q6MAC7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways